PURIFICATION, CHARACTERIZATION AND RECONSTITUTION OF CMP-N-ACETYLNEURAMINATE HYDROXYLASE FROM MOUSE-LIVER

被引：14

作者：

SCHNECKENBURGER, P ^{[1
]}

SHAW, L ^{[1
]}

SCHAUER, R ^{[1
]}

机构：

[1] CHRISTIAN ALBRECHTS UNIV KIEL,INST BIOCHEM,D-24098 KIEL,GERMANY

来源：

GLYCOCONJUGATE JOURNAL | 1994年 / 11卷 / 03期

关键词：

SIALIC ACID; N-GLYCOLOYLNEURAMINIC ACID; HYDROXYLASE; PROTEIN PURIFICATION; CYTOCHROME B(5); ELECTRON TRANSFER; ENZYME SYSTEM RECONSTITUTION;

D O I：

10.1007/BF00731218

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

CMP-N-acetylneuraminate hydroxylase was isolated from mouse liver high speed supernatant with a yield of 0.4% and an apparent 1000-fold purification. The enzyme is a monomeric protein with a molecular weight of 66 kDa, as determined by gel filtration and SDS-PAGE. The hydroxylase system was reconstituted with Triton X-100-solubilized mouse liver microsomes and purified soluble or microsomal forms of cytochrome b(5) reductase and cytochrome b(5). The systems were characterized in detail and kinetic parameters for each system were determined.

引用

页码：194 / 203

页数：10

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